@article {2525,
	title = {Detection and assignment of phosphoserine and phosphothreonine residues by C-13-P-31 spin-echo difference NMR spectroscopy},
	journal = {Journal of Biomolecular Nmr},
	volume = {43},
	number = {1},
	year = {2009},
	note = {ISI Document Delivery No.: 379QKTimes Cited: 0Cited Reference Count: 31McIntosh, Lawrence P. Kang, Hyun-Seo Okon, Mark Nelson, Mary L. Graves, Barbara J. Brutscher, Bernhard},
	month = {Jan},
	pages = {31-37},
	type = {Article},
	abstract = {A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in C-13- or C-13/N-15-labeled proteins. By exploiting modest (similar to 5 Hz) 2- and 3-bond C-13-P-31 scalar couplings, the aliphatic H-1-C-13 signals from phosphoserines and phosphothreonines can be detected selectively in a P-31 spin-echo difference constant time H-1-C-13 HSQC spectrum. Inclusion of the same P-31 spin-echo element within the C-13 frequency editing period of an intraHNCA or HN(CO)CA experiment allows identification of the amide H-1(N) and N-15 signals of residues (i) for which C-13(alpha)(i) or C-13(alpha)(i - 1), respectively, are coupled to a phosphate. Furthermore, P-31 resonance assignments can be obtained by applying selective low power cw P-31 decoupling during the spin-echo period. The approach is demonstrated using a PNT domain containing fragment of the transcription factor Ets-1, phosphorylated in vitro at Thr38 and Ser41 with the MAP kinase ERK2.},
	keywords = {ASSIGNMENT, CENTER-DOT-OP, CONSTANT-TIME, Ets-1, MAP kinase, NUCLEIC-ACIDS, OP HYDROGEN-BONDS, P-31-C-13 scalar coupling, Phosphoprotein, PHOSPHORYLATION, POINTED DOMAIN, PROTEIN, QUANTITATIVE J-CORRELATION, RESONANCE, SCALAR COUPLINGS, TRANSCRIPTION FACTOR},
	isbn = {0925-2738},
	url = {<Go to ISI>://000261411100004},
	author = {McIntosh, L. P. and Kang, H. S. and Okon, M. and Nelson, M. L. and Graves, B. J. and Brutscher, B.}
}
@article {1165,
	title = {The structural and dynamic basis of Ets-1 DNA binding autoinhibition},
	journal = {Journal of Biological Chemistry},
	volume = {280},
	number = {8},
	year = {2005},
	note = {ISI Document Delivery No.: 902DTTimes Cited: 19Cited Reference Count: 73},
	month = {Feb},
	pages = {7088-7099},
	type = {Article},
	abstract = {The transcription factor Ets-1 is regulated by the allosteric coupling of DNA binding with the unfolding of an alpha-helix (HI-1) within an autoinhibitory module. To understand the structural and dynamic basis for this autoinhibition, we have used NAIR spectroscopy to characterize Ets-1DeltaN301, a partially inhibited fragment of Ets-1. The NMR-derived Ets-1DeltaN301 structure reveals that the autoinhibitory module is formed predominantly by the hydrophobic packing of helices from the N-terminal (HI-1, HI-2) and C-terminal (114, 115) inhibitory sequences, along with H1 of the intervening DNA binding ETS domain. The intramolecular interactions made by HI-1 in Ets-1DeltaN301 are similar to the intermolecular contacts observed in the crystal structure of an Ets-1DeltaN300 dimer, confirming that the latter represents a domain-swapped species. N-15 relaxation studies demonstrate that the backbone of the N-terminal inhibitory sequence is mobile on the nanosecond-picosecond and millisecond-microsecond time scales. Furthermore, hydrogen exchange measurements reveal that amide protons in helices HI-I and HI-2 exchange with water at rates only similar to15- and similar to75-fold slower, respectively, than predicted for an unfolded polypeptide. These findings indicate that inhibitory helices are only marginally stable even in the absence of DNA. The energetic coupling of DNA binding with the facile unfolding of the labile HI-1 provides a mechanism for modulating Ets-1 DNA binding activity via protein partnerships, post-translational modifications, or mutations. Ets-1 autoinhibition illustrates how conformational equilibria within structural domains can regulate macromolecular interactions.},
	keywords = {BACKBONE DYNAMICS, CHEMICAL-EXCHANGE, DIPOLAR COUPLINGS, Ets-1, GROUP HYDROGEN-EXCHANGE, HIGH-RESOLUTION, MURINE, N-15 NMR RELAXATION, POINTED DOMAIN, SECONDARY STRUCTURE, SIDE-CHAINS},
	isbn = {0021-9258},
	url = {<Go to ISI>://000227332700099},
	author = {Lee, G. M. and Donaldson, L. W. and Pufall, M. A. and Kang, H. S. and Pot, I. and Graves, B. J. and McIntosh, L. P.}
}
@article {438,
	title = {Letter to the Editor: Chemical shift and secondary structure conservation of the PNT/SAM domains from the Ets family of transcription factors},
	journal = {Journal of Biomolecular Nmr},
	volume = {24},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 603GNTimes Cited: 6Cited Reference Count: 9},
	month = {Sep},
	pages = {71-72},
	type = {Letter},
	keywords = {Erg, Ets-1, GABP alpha, PNT domain, PROTEINS, SAM domain, secondary chemical shift, STEREOSPECIFIC ASSIGNMENT},
	isbn = {0925-2738},
	url = {<Go to ISI>://000178550700008},
	author = {Mackereth, C. D. and Scharpf, M. and Gentile, L. N. and McIntosh, L. P.}
}
